The formation of the peptide bond in a template-directed reaction is being investigated. Amino acids (initially alanine) are attached as esters to oligonucleotides in such a way that when the latter complex with a template nucleic acid, peptide bond formation should take place by virtue of the juxtaposition of the amino group of one amino acid with the ester carbonyl group of another. The oligonucleotides consist of all (D)-ribonucleosides, and the peptides that result from this reaction will be examined to see if they contain a preponderance of one of the enantiomers of alanine. Appropriate control reactions will be run to check that the peptide bond formation is indeed taking place in the complex. In other work, the formation and hydrolysis of 2',5' and 3',5' internucleotide bonds in a double (as opposed to a triple) helix will be further studied.